Identification and functional characterization of protein kinase A phosphorylation sites in the major lipolytic protein, adipose triglyceride lipase.

@article{Pagnon2012IdentificationAF,
  title={Identification and functional characterization of protein kinase A phosphorylation sites in the major lipolytic protein, adipose triglyceride lipase.},
  author={Joanne C Pagnon and Maria Matzaris and Romana Stark and Ruth Carla Meex and Stuart Lance Macaulay and W. Kent Brown and Paul E O'Brien and Tony Tiganis and Matthew J Watt},
  journal={Endocrinology},
  year={2012},
  volume={153 9},
  pages={4278-89}
}
Catecholamine-stimulated lipolysis occurs by activating adenylate cyclase and raising cAMP levels, thereby increasing protein kinase A (PKA) activity. This results in phosphorylation and modulated activity of several key lipolytic proteins. Adipose triglyceride lipase (ATGL) is the primary lipase for the initial step in triacylglycerol hydrolysis, and ATGL activity is increased during stimulated lipolysis. Here, we demonstrate that murine ATGL is phosphorylated by PKA at several serine residues… CONTINUE READING

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